Structure of PDB 1zg3 Chain A

Receptor sequence

>1zg3A (length=358) Species: 3880 (Medicago truncatula)

GSEESELYHAQIHLYKHVYNFVSSMALKSAMELGIADAIHNHGKPMTLSE
LASSLKLHPSKVNILHRFLRLLTHNGFFAKTIVKGKEGDEEEEIAYSLTP
PSKLLISGKPTCLSSIVKGALHPSSLDMWSSSKKWFNEDKEQTLFECATG
ESFWDFLNKDSESSTLSMFQDAMASDSRMFKLVLQENKRVFEGLESLVDV
GGGTGGVTKLIHEIFPHLKCTVFDQPQVVGNLTGNENLNFVGGDMFKSIP
SADAVLLKWVLHDWNDEQSLKILKNSKEAISHKGKDGKVIIIDISIDETS
DDRGLTELQLDYDLVMLTMFLGKERTKQEWEKLIYDAGFSSYKITPISGF
KSLIEVYP

3D structure

• PDB: 1zg3 Structural basis for dual functionality of isoflavonoid O-methyltransferases in the evolution of plant defense responses.
• Chain: A
• Resolution: 2.35 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): H268 D269 D299 E330
• Catalytic site (residue number reindexed from 1): H262 D263 D293 E324
• Enzyme Commision number: 2.1.1.212: 2,7,4'-trihydroxyisoflavanone 4'-O-methyltransferase.
  2.1.1.46: isoflavone 4'-O-methyltransferase.

Interaction with ligand

Site #	Ligand	Ligand chain	Binding residues on receptor (original residue number in PDB)	Binding residues on receptor (residue number reindexed from 1)	Binding affinity
BS01	2HI	A	G125 A126 A178 M179 Y318 M325 F326	G119 A120 A172 M173 Y312 M319 F320
BS02	SAH	A	G207 V213 D230 Q231 D250 M251 K264	G201 V207 D224 Q225 D244 M245 K258

Gene Ontology

Molecular Function

• GO:0008168 methyltransferase activity
• GO:0008171 O-methyltransferase activity
• GO:0008757 S-adenosylmethionine-dependent methyltransferase activity
• GO:0030746 isoflavone 4'-O-methyltransferase activity
• GO:0046983 protein dimerization activity
• GO:0102670 2,7,4'-trihydroxyisoflavanone-4'-O-methyltransferase activity

Biological Process

• GO:0032259 methylation

External links

• PDB: RCSB:1zg3, PDBe:1zg3, PDBj:1zg3
• PDBsum: 1zg3
• PubMed: 17172354
• UniProt: Q29U70|I4OMT_MEDTR Isoflavone 4'-O-methyltransferase (Gene Name=HI4'OMT)